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pi 4 5 p2 levels  (Echelon Biosciences)


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    Structured Review

    Echelon Biosciences pi 4 5 p2 levels
    Pi 4 5 P2 Levels, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pi 4 5 p2 levels/product/Echelon Biosciences
    Average 93 stars, based on 1 article reviews
    pi 4 5 p2 levels - by Bioz Stars, 2025-02
    93/100 stars

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    Echelon Biosciences dic4 pi 4 5 p2
    Phospholipid-binding abilities of Arap3-PH1 domain analyzed using liposome pull-down assay and SPR measurements. ( A ) Schematic representation of human Arap3 protein. The first PH domain of Arap3 is marked in cyan. ( B ) Sequence alignment of Arap3-PH1 orthologs in vertebrates and human Arap1-PH1, Arap2-PH1. Sequence accession number in the Uniprot database are: human, Q8WWN8; bovine, E1BBA0; mouse, Q8R5G7; zebrafish, A0A140LH27; human Arap1, Q96P48; human Arap2, Q8WZ64. Alignment was performed using Clustal X and illustrated with ESPript 3.0. Strictly conserved (white letters filled with red color) and conservatively substituted (red letters with blue box) residues are denoted. The secondary structure element for human Arap3-PH1 is labeled on the top. The KXnQXR motif are marked by black dots. ( C ) Arap3-PH1 (20 μg) mixed with liposomes (640 μg) composed of 98% PC as the fixed component and 2% of specific phospholipids, respectively. Proteins in the absence of liposome were used as a control. After centrifugation, the pellet (P) and supernatant (S) were analyzed by SDS/PAGE and Coomassie. ( D ) SPR measurements of the binding affinities of the Arap3-PH1 domain for <t>diC4-PI(3,4,5)P3</t> and diC4-PI(4,5)P2. The upper panel shows representative sensorgrams of diC4-PI(3,4,5)P3 (left) and diC4-PI(4,5)P2 (right) when mixed with Arap3-PH1. Data were collected by injecting increasing concentrations of diC4-PI(3,4,5)P3 and diC4-PI(4,5)P2 samples over Arap3-PH1 proteins immobilized on the surface of a CM5 biochip. The lower panel shows representative binding curves fitting for diC4-PI(3,4,5)P3 (left) and diC4-PI(4,5)P2 (right) during their interaction with Arap3-PH1. A one-site binding model was utilized to fit the curves. The experiment was carried out in triplicate. The KD value is presented as mean ± SD, n = 3.
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    Image Search Results


    Phospholipid-binding abilities of Arap3-PH1 domain analyzed using liposome pull-down assay and SPR measurements. ( A ) Schematic representation of human Arap3 protein. The first PH domain of Arap3 is marked in cyan. ( B ) Sequence alignment of Arap3-PH1 orthologs in vertebrates and human Arap1-PH1, Arap2-PH1. Sequence accession number in the Uniprot database are: human, Q8WWN8; bovine, E1BBA0; mouse, Q8R5G7; zebrafish, A0A140LH27; human Arap1, Q96P48; human Arap2, Q8WZ64. Alignment was performed using Clustal X and illustrated with ESPript 3.0. Strictly conserved (white letters filled with red color) and conservatively substituted (red letters with blue box) residues are denoted. The secondary structure element for human Arap3-PH1 is labeled on the top. The KXnQXR motif are marked by black dots. ( C ) Arap3-PH1 (20 μg) mixed with liposomes (640 μg) composed of 98% PC as the fixed component and 2% of specific phospholipids, respectively. Proteins in the absence of liposome were used as a control. After centrifugation, the pellet (P) and supernatant (S) were analyzed by SDS/PAGE and Coomassie. ( D ) SPR measurements of the binding affinities of the Arap3-PH1 domain for diC4-PI(3,4,5)P3 and diC4-PI(4,5)P2. The upper panel shows representative sensorgrams of diC4-PI(3,4,5)P3 (left) and diC4-PI(4,5)P2 (right) when mixed with Arap3-PH1. Data were collected by injecting increasing concentrations of diC4-PI(3,4,5)P3 and diC4-PI(4,5)P2 samples over Arap3-PH1 proteins immobilized on the surface of a CM5 biochip. The lower panel shows representative binding curves fitting for diC4-PI(3,4,5)P3 (left) and diC4-PI(4,5)P2 (right) during their interaction with Arap3-PH1. A one-site binding model was utilized to fit the curves. The experiment was carried out in triplicate. The KD value is presented as mean ± SD, n = 3.

    Journal: International Journal of Molecular Sciences

    Article Title: Structural Insights Uncover the Specific Phosphoinositide Recognition by the PH1 Domain of Arap3

    doi: 10.3390/ijms24021125

    Figure Lengend Snippet: Phospholipid-binding abilities of Arap3-PH1 domain analyzed using liposome pull-down assay and SPR measurements. ( A ) Schematic representation of human Arap3 protein. The first PH domain of Arap3 is marked in cyan. ( B ) Sequence alignment of Arap3-PH1 orthologs in vertebrates and human Arap1-PH1, Arap2-PH1. Sequence accession number in the Uniprot database are: human, Q8WWN8; bovine, E1BBA0; mouse, Q8R5G7; zebrafish, A0A140LH27; human Arap1, Q96P48; human Arap2, Q8WZ64. Alignment was performed using Clustal X and illustrated with ESPript 3.0. Strictly conserved (white letters filled with red color) and conservatively substituted (red letters with blue box) residues are denoted. The secondary structure element for human Arap3-PH1 is labeled on the top. The KXnQXR motif are marked by black dots. ( C ) Arap3-PH1 (20 μg) mixed with liposomes (640 μg) composed of 98% PC as the fixed component and 2% of specific phospholipids, respectively. Proteins in the absence of liposome were used as a control. After centrifugation, the pellet (P) and supernatant (S) were analyzed by SDS/PAGE and Coomassie. ( D ) SPR measurements of the binding affinities of the Arap3-PH1 domain for diC4-PI(3,4,5)P3 and diC4-PI(4,5)P2. The upper panel shows representative sensorgrams of diC4-PI(3,4,5)P3 (left) and diC4-PI(4,5)P2 (right) when mixed with Arap3-PH1. Data were collected by injecting increasing concentrations of diC4-PI(3,4,5)P3 and diC4-PI(4,5)P2 samples over Arap3-PH1 proteins immobilized on the surface of a CM5 biochip. The lower panel shows representative binding curves fitting for diC4-PI(3,4,5)P3 (left) and diC4-PI(4,5)P2 (right) during their interaction with Arap3-PH1. A one-site binding model was utilized to fit the curves. The experiment was carried out in triplicate. The KD value is presented as mean ± SD, n = 3.

    Article Snippet: DiC4-PI(3,4,5)P3 (Echelon, Salt Lake City, UT, USA) were diluted from 75 μM to 1.172 μM as 1:2 dilution series and diC4-PI(4,5)P2 (Echelon, USA) were diluted from 600 μM to 4.688 μM.

    Techniques: Binding Assay, Pull Down Assay, Sequencing, Labeling, Liposomes, Control, Centrifugation, SDS Page

    Crystallographic data collection and refinement statistics.

    Journal: International Journal of Molecular Sciences

    Article Title: Structural Insights Uncover the Specific Phosphoinositide Recognition by the PH1 Domain of Arap3

    doi: 10.3390/ijms24021125

    Figure Lengend Snippet: Crystallographic data collection and refinement statistics.

    Article Snippet: DiC4-PI(3,4,5)P3 (Echelon, Salt Lake City, UT, USA) were diluted from 75 μM to 1.172 μM as 1:2 dilution series and diC4-PI(4,5)P2 (Echelon, USA) were diluted from 600 μM to 4.688 μM.

    Techniques:

    Structure of the Arap3-PH1 domain in complex with diC4-PI(3,4,5)P3. ( A ) Cartoon diagram of Arap3-PH1 complexed with diC4-PI(3,4,5)P3. Arap3-PH1 is colored turquoise, with secondary structures labeled. The loops of β1/β2 and β6/β7 that interact directly with diC4-PI(3,4,5)P3 are colored blue. The diC4-PI(3,4,5)P3 (gold) is shown in stick mode. ( B ) Surface electrostatic potential of Arap3-PH1 complexed with diC4-PI(3,4,5)P3. Blue areas, positive; red areas, negative. ( C ) Detailed interactions of the diC4-PI(3,4,5)P3 with Arap3-PH1 domain. The side chains of crucial residues are shown in stick mode and labeled, respectively. The phosphate groups on diC4-PI(3,4,5)P3 are also labeled. Selected hydrogen bonds or salt bridges are shown as dotted lines.

    Journal: International Journal of Molecular Sciences

    Article Title: Structural Insights Uncover the Specific Phosphoinositide Recognition by the PH1 Domain of Arap3

    doi: 10.3390/ijms24021125

    Figure Lengend Snippet: Structure of the Arap3-PH1 domain in complex with diC4-PI(3,4,5)P3. ( A ) Cartoon diagram of Arap3-PH1 complexed with diC4-PI(3,4,5)P3. Arap3-PH1 is colored turquoise, with secondary structures labeled. The loops of β1/β2 and β6/β7 that interact directly with diC4-PI(3,4,5)P3 are colored blue. The diC4-PI(3,4,5)P3 (gold) is shown in stick mode. ( B ) Surface electrostatic potential of Arap3-PH1 complexed with diC4-PI(3,4,5)P3. Blue areas, positive; red areas, negative. ( C ) Detailed interactions of the diC4-PI(3,4,5)P3 with Arap3-PH1 domain. The side chains of crucial residues are shown in stick mode and labeled, respectively. The phosphate groups on diC4-PI(3,4,5)P3 are also labeled. Selected hydrogen bonds or salt bridges are shown as dotted lines.

    Article Snippet: DiC4-PI(3,4,5)P3 (Echelon, Salt Lake City, UT, USA) were diluted from 75 μM to 1.172 μM as 1:2 dilution series and diC4-PI(4,5)P2 (Echelon, USA) were diluted from 600 μM to 4.688 μM.

    Techniques: Labeling

    The binding interfaces of Arap3-PH1 for diC4-PI(3,4,5)P3 and diC4-PI(4,5)P2 revealed by NMR titration. ( A ) Overlay of 1 H- 15 N HSQC spectra of Arap3-PH1 in the absence (black) and in the increasing amounts of diC4-PI(3,4,5)P3. The molar ratios of the protein to diC4-PI(3,4,5)P3 are shown in the inset: 1:0 (black), 1:0.25 (turquoise), 1:0.5 (lime green), 1:0.75 (orange), 1:1 (pink) and 1:1.25 (red). ( B ) Overlay of 1 H- 15 N HSQC spectra of Arap3-PH1 in the absence (black) and in increasing amounts of diC4-PI(4,5)P2. The molar ratios of the protein to diC4-PI(4,5)P2 are shown in the inset: 1:0 (black), 1:0.5 (royal blue), 1:1 (turquoise), 1:2 (lime green), 1:4 (orange), 1:6 (pink) and 1:8 (red). ( C ) The chemical shift perturbations (CSPs) of each residue during NMR titrations (up, diC4-PI(3,4,5)P3 titration; down, diC4-PI(4,5)P2 titration) are calculated and shown with the secondary elements on top. White dots indicate pro residues. Black dots indicate residues with no data. The mean value and the mean value plus one standard deviation are indicated by dash and solid lines, respectively. Residues with CSPs between mean value and mean value plus one standard deviation are colored gold, and above mean value plus one standard deviations are colored red. ( D , E ) Surface representations of the Arap3-PH1 structure with the perturbed residues upon binding to diC4-PI(3,4,5)P3 and diC4-PI(4,5)P2 are colored and labeled.

    Journal: International Journal of Molecular Sciences

    Article Title: Structural Insights Uncover the Specific Phosphoinositide Recognition by the PH1 Domain of Arap3

    doi: 10.3390/ijms24021125

    Figure Lengend Snippet: The binding interfaces of Arap3-PH1 for diC4-PI(3,4,5)P3 and diC4-PI(4,5)P2 revealed by NMR titration. ( A ) Overlay of 1 H- 15 N HSQC spectra of Arap3-PH1 in the absence (black) and in the increasing amounts of diC4-PI(3,4,5)P3. The molar ratios of the protein to diC4-PI(3,4,5)P3 are shown in the inset: 1:0 (black), 1:0.25 (turquoise), 1:0.5 (lime green), 1:0.75 (orange), 1:1 (pink) and 1:1.25 (red). ( B ) Overlay of 1 H- 15 N HSQC spectra of Arap3-PH1 in the absence (black) and in increasing amounts of diC4-PI(4,5)P2. The molar ratios of the protein to diC4-PI(4,5)P2 are shown in the inset: 1:0 (black), 1:0.5 (royal blue), 1:1 (turquoise), 1:2 (lime green), 1:4 (orange), 1:6 (pink) and 1:8 (red). ( C ) The chemical shift perturbations (CSPs) of each residue during NMR titrations (up, diC4-PI(3,4,5)P3 titration; down, diC4-PI(4,5)P2 titration) are calculated and shown with the secondary elements on top. White dots indicate pro residues. Black dots indicate residues with no data. The mean value and the mean value plus one standard deviation are indicated by dash and solid lines, respectively. Residues with CSPs between mean value and mean value plus one standard deviation are colored gold, and above mean value plus one standard deviations are colored red. ( D , E ) Surface representations of the Arap3-PH1 structure with the perturbed residues upon binding to diC4-PI(3,4,5)P3 and diC4-PI(4,5)P2 are colored and labeled.

    Article Snippet: DiC4-PI(3,4,5)P3 (Echelon, Salt Lake City, UT, USA) were diluted from 75 μM to 1.172 μM as 1:2 dilution series and diC4-PI(4,5)P2 (Echelon, USA) were diluted from 600 μM to 4.688 μM.

    Techniques: Binding Assay, Titration, Residue, Standard Deviation, Labeling

    Components of T-buffer and S-buffer.

    Journal: Science Advances

    Article Title: The membrane-actin linker ezrin acts as a sliding anchor

    doi: 10.1126/sciadv.abo2779

    Figure Lengend Snippet: Components of T-buffer and S-buffer.

    Article Snippet: PI(4,5)P 2 diC4 (P-4504, Echelon Biosciences) was either dissolved directly in F-buffer and stored at −80°C (as aliquots or as stock) or dissolved in ultrapure water, stored at −80°C, and diluted 20× in F-buffer before usage (see the “Tightrope assay” section for details of usage).

    Techniques: